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Recent Photos from the National Institute of General Medical Sciences
(NIGMS)

2010 Photos

Long-time NIGMS grantee Ei-ichi Negishi shared the 2010 Nobel Prize in chemistry with Richard F. Heck and Akira Suzuki for developing carbon-carbon bond-forming methods. The methods, now widely used in the production of substances ranging from medicines to plastics, let scientists bring two molecules very close together. This allows the molecules to couple, form a compound with a new carbon-carbon bond, release the product and be ready for another cycle. To date, NIGMS has supported the research of 74 Nobel Prize winners. (Structure image courtesy of PubChem)lo-res | hi-res

2009 Photos

NIH
grantees Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E.
Yonath shared the 2009 Nobel Prize in chemistry for their “studies
of the structure and function of the ribosome.” Ribosomes
are the molecular factories that manufacture proteins in humans
and other organisms. Knowing the structure and function of the
ribosome has helped us understand one of life's most fundamental
processes and manipulate it—many of our antibiotics work
by disrupting bacterial ribosomes. (Image courtesy of Catherine
Lawson, Rutgers University, and the RCSB Protein Data Bank.)lo-res | hi-res

NIH
grantees Elizabeth H. Blackburn, Carol W. Greider, and Jack W.
Szostak shared the 2009 Nobel Prize in physiology or medicine for
their discovery of "how chromosomes are protected by telomeres
and the enzyme telomerase." Like the plastic tips of shoelaces,
telomeres protect chromosomes and the genetic information they
contain. We now know that these chromosomal caps play critical
roles in human health and disease. (Image courtesy of Hesed Padilla-Nash
and Thomas Ried.)lo-res | hi-res

2008 Photos

NIH grantees Martin Chalfie and Roger Y. Tsien shared the 2008 Nobel Prize in
chemistry with former grantee Osamu Shimomura for their groundbreaking work on
green fluorescent protein. This naturally glowing protein found in jellyfish
has become a powerful tool for studying molecules inside living cells. (Image
courtesy of Roger Tsien, Univeristy of California, San Diego)lo-res | hi-res

2007 Photos

This
model of the enzyme nicotinic acid phosphoribosyltransferase
is one of more than 2,000 protein structures solved as part
of NIGMS's Protein Structure Initiative. Although the enzyme
is from a bacterium, its amino acid sequence suggests that
it is structurally similar to a clinically important human
protein called B-cell colony enhancing factor. (Image courtesy
of Berkeley Structural Genomics Center) lo-res | hi-res

Hailed
as a scientific breakthrough, NIGMS grantee James Thomson used
human skin cells to create ones that appear to be indistinguishable
from embryonic stem cells. In 2007, Thomson and his colleagues
reported that they'd reset the skin cells to the embryonic
state by supplying them with 4 genes, giving them the potential
to become any of the 220 cell types in the body. The new technique
is expected to bring stem cells within easier reach of more
scientists, providing them with better models for studying
many human diseases and possibly speeding the advent of cell-based
therapies for conditions such as diabetes and arthritis. This
work also was supported by NIH's National Center for Research
Resources (NCRR). (Image courtesy of Junying Yu, University
of Wisconsin-Madison)lo-res | hi-res